scholarly journals Mechanism of Calmodulin Recognition of the Binding Domain of Isoform 1b of the Plasma Membrane Ca2+-ATPase:  Kinetic Pathway and Effects of Methionine Oxidation†

Biochemistry ◽  
2007 ◽  
Vol 46 (13) ◽  
pp. 4045-4054 ◽  
Author(s):  
Brian D. Slaughter ◽  
Ramona J. Bieber Urbauer ◽  
Jeffrey L. Urbauer ◽  
Carey K. Johnson
Keyword(s):  
Plasma Membrane ◽  
Binding Domain ◽  
Methionine Oxidation

scholarly journals The Calmodulin Binding Domain of the Plasma Membrane Ca2+ Pump Interacts Both with Calmodulin and with Another Part of the Pump

1989 ◽  
Vol 264 (21) ◽  
pp. 12313-12321 ◽  
Author(s):  
A Enyedi ◽  
T Vorherr ◽  
P James ◽  
D J McCormick ◽  
A G Filoteo ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Domain ◽  
Calmodulin Binding

scholarly journals Calmodulin Wraps around Its Binding Domain in the Plasma Membrane Ca2+Pump Anchored by a Novel 18-1 Motif

2009 ◽  
Vol 285 (6) ◽  
pp. 4015-4024 ◽  
Author(s):  
Nenad Juranic ◽  
Elena Atanasova ◽  
Adelaida G. Filoteo ◽  
Slobodan Macura ◽  
Franklyn G. Prendergast ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Domain

p-Nitrophenylphosphatase Activity Catalyzed by Plasma Membrane (Ca2++Mg2+)ATPase: Correlation with Structural Changes Modulated by Glycerol and Ca2+

2001 ◽  
Vol 21 (1) ◽  
pp. 25-32 ◽  
Author(s):  
Gutemberg G. Alves ◽  
Luis Maurício T. R. Lima ◽  
Maely P. Fávero-Retto ◽  
Adriana P. Lemos ◽  
Carlos E. Peres-Sampaio ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Synergistic Effect ◽  
Phosphatase Activity ◽  
Structural Changes ◽  
Center Of Mass ◽  
Binding Domain ◽  
Dependent Manner ◽  
Dose Dependent ◽  
Substrate Binding Domain

The plasma membrane (Ca2++Mg2+)ATPase hydrolyzes pseudo-substrates such as p-nitrophenylphosphate. Except when calmodulin is present, Ca2+ ions inhibit the p-nitrophenylphosphatase activity. In this report it is shown that, in the presence of glycerol, Ca2+ strongly stimulates phosphatase activity in a dose-dependent manner. The glycerol- and Ca2+-induced increase in activity is correlated with modifications in the spectral center of mass (average emission wavenumber) of the intrinsic fluorescence of the enzyme. It is concluded that the synergistic effect of glycerol and Ca2+ is related to opposite long-term hydration effects on the substrate binding domain and the Ca2+ binding domain.

Interaction of calmodulin with the calmodulin binding domain of the plasma membrane calcium pump

Biochemistry ◽  
1990 ◽  
Vol 29 (2) ◽  
pp. 355-365 ◽  
Author(s):  
Thomas Vorherr ◽  
Peter James ◽  
Joachim Krebs ◽  
Agnes Enyedi ◽  
Daniel J. McCormick ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Domain ◽  
Calcium Pump ◽  
Calmodulin Binding ◽  
Plasma Membrane Calcium Pump

scholarly journals The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain

Metallomics ◽  
2015 ◽  
Vol 7 (9) ◽  
pp. 1319-1330 ◽  
Author(s):  
Elizabeth M. Bafaro ◽  
Sagar Antala ◽  
Tuong-Vi Nguyen ◽  
Stephen P. Dzul ◽  
Brian Doyon ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Binding Domain ◽  
Zinc Binding ◽  
Plasma Membrane Protein ◽  
Intracellular Loop ◽  
Intrinsically Disordered ◽  
Zinc Binding Domain

The human (h) ZIP4 transporter is a plasma membrane protein which functions to increase the cytosolic concentration of zinc.

scholarly journals The Interaction of JRAB/MICAL-L2 with Rab8 and Rab13 Coordinates the Assembly of Tight Junctions and Adherens Junctions

2008 ◽  
Vol 19 (3) ◽  
pp. 971-983 ◽  
Author(s):  
Rie Yamamura ◽  
Noriyuki Nishimura ◽  
Hiroyoshi Nakatsuji ◽  
Seiji Arase ◽  
Takuya Sasaki
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Tight Junctions ◽  
Binding Protein ◽  
Adherens Junctions ◽  
Binding Domain ◽  
Endocytic Recycling ◽  
E Cadherin

The assembly of tight junctions (TJs) and adherens junctions (AJs) is regulated by the transport of integral TJ and AJ proteins to and/or from the plasma membrane (PM) and it is tightly coordinated in epithelial cells. We previously reported that Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) mediated the endocytic recycling of an integral TJ protein occludin and the formation of functional TJs. Here, we investigated the role of Rab13 and JRAB/MICAL-L2 in the transport of other integral TJ and AJ proteins claudin-1 and E-cadherin to the PM by using a Ca2+-switch model. Although knockdown of Rab13 specifically suppressed claudin-1 and occludin but not E-cadherin transport, knockdown of JRAB/MICAL-L2 and expression of its Rab13-binding domain (JRAB/MICAL-L2-C) inhibited claudin-1, occludin, and E-cadherin transport. We then identified Rab8 as another JRAB/MICAL-L2-C-binding protein. Knockdown of Rab8 inhibited the Rab13-independent transport of E-cadherin to the PM. Rab8 and Rab13 competed with each other for the binding to JRAB/MICAL-L2 and functionally associated with JRAB/MICAL-L2 at the perinuclear recycling/storage compartments and PM, respectively. These results suggest that the interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of AJs and TJs.

scholarly journals Protein Kinase C Phosphorylates Plasma Membrane Ca2+Pump Isoform 4a at Its Calmodulin Binding Domain

1999 ◽  
Vol 274 (1) ◽  
pp. 527-531 ◽  
Author(s):  
Anil K. Verma ◽  
Katalin Paszty ◽  
Adelaida G. Filoteo ◽  
John T. Penniston ◽  
Agnes Enyedi
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Domain ◽  
Calmodulin Binding ◽  
Kinase C

scholarly journals AS160 Phosphotyrosine-binding Domain Constructs Inhibit Insulin-stimulated GLUT4 Vesicle Fusion with the Plasma Membrane

2011 ◽  
Vol 286 (19) ◽  
pp. 16574-16582 ◽  
Author(s):  
Françoise Koumanov ◽  
Judith D. Richardson ◽  
Beverley A. Murrow ◽  
Geoffrey D. Holman
Keyword(s):  
Plasma Membrane ◽  
Vesicle Fusion ◽  
Binding Domain ◽  
Phosphotyrosine Binding Domain
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